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Archaeal (per)chlorate reduction at high temperature: an interplay of biotic and abiotic reactions (2013)

M. G. Liebensteiner ; M. W. Pinkse ; P. J. Schaap ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 340(6128): 85-7. doi: 10.1126/science.1233957.

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Publication Date: 2013-04-06

Description: Perchlorate and chlorate anions [(per)chlorate] exist in the environment from natural and anthropogenic sources, where they can serve as electron acceptors for bacteria. We performed growth experiments combined with genomic and proteomic analyses of the hyperthermophile Archaeoglobus fulgidus that show (per)chlorate reduction also extends into the archaeal domain of life. The (per)chlorate reduction pathway in A. fulgidus relies on molybdo-enzymes that have similarity with bacterial enzymes; however, chlorite is not enzymatically split into chloride and oxygen. Evidence suggests that it is eliminated by an interplay of abiotic and biotic redox reactions involving sulfur compounds. Biological (per)chlorate reduction by ancient archaea at high temperature may have prevented accumulation of perchlorate in early terrestrial environments and consequently given rise to oxidizing conditions on Earth before the rise of oxygenic photosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liebensteiner, Martin G -- Pinkse, Martijn W H -- Schaap, Peter J -- Stams, Alfons J M -- Lomans, Bart P -- New York, N.Y. -- Science. 2013 Apr 5;340(6128):85-7. doi: 10.1126/science.1233957.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Microbiology, Wageningen University, Dreijenplein 10, 6703 HB Wageningen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23559251" target="_blank"〉PubMed〈/a〉

Keywords: Archaeoglobus fulgidus/*enzymology ; Metabolic Networks and Pathways ; Oxidation-Reduction ; Oxidoreductases/metabolism ; Perchlorates/*metabolism ; Temperature

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics

Published by American Association for the Advancement of Science (AAAS)

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Identification of regulatory mutants of Aspergillus aculeatus affected in rhamnogalacturonan hydrolase expression (1996)

Suykerbuyk, M. E. G. ; van de Vondervoort, P. J. I. ; Schaap, P. J. ; [et al.]

Springer

Current genetics 30 (1996), S. 439-446

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ISSN: 1432-0983

Keywords: Key words Aspergillus aculeatus ; Rhamnogalacturonan hydrolase ; Reporter enzyme ; Mutagenesis

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Rhamnogalacturonan hydrolase expression in A. aculeatus can be induced by pectin, but also by a combination of two constituent monosaccharides of pectin, rhamnose and galacturonic acid. The rhgA promoter was fused to the A. niger glucose oxidase coding sequence and a single copy of the hybrid gene was integrated at the rhgA locus in the genome of A. aculeatus. The gene product was subsequently used as reporter in a screening assay for the selection of rhamnogalacturonan hydrolase-overproducing mutant strains. At least four of the mutations were recessive and could be assigned to different loci. One mutation (rgr25) showed linkage with the rhgA locus. Inducible rhamnogalacturonan hydrolase expression levels of about 5–10 times that in the wild-type were found in the mutants rgr48, rgr25 and rgr34 after growth on a combination of rhamnose and galacturonic acid with or without fructose as a carbon source. In mutant rgr48 elevated levels of rhgA transcription were found.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002940050154

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Molecular characterization of the glnA gene encoding glutamine synthetase from the edible mushroom Agaricus bisporus (1997)

Kersten, M. A. S. H. ; Müller, Y. ; Op den Camp, H. J. M. ; [et al.]

Springer

Molecular genetics and genomics 256 (1997), S. 179-186

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ISSN: 1617-4623

Keywords: Key wordsAgaricus bisporus ; Glutamine synthetase ; Molecular cloning ; Gene structure ; Mushroom

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The gene encoding glutamine synthetase (glnA) was isolated from an Agaricus bisporus H39 recombinant λ phage library. The deduced A. bisporus glutamine synthetase amino acid sequence contains 354 residues. The amino acid sequence is very similar to that derived from the gene coding for glutamine synthetase of the yeast Saccharomyces cerevisiae. The open reading frame is interrupted by four introns. Northern analysis revealed that transcription of the gene is repressed upon addition of ammonium to the culture but the repression was not as strong as that of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA). Enzyme activities are low in the presence of ammonium, glutamine and albumin and do not correlate with the mRNA levels revealed by Northern analysis. This suggests that glutamine synthetase expression in A. bisporus is also post-transcriptionally regulated by the nitrogen source.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/PL00008612

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NAD+-dependent glutamate dehydrogenase of the edible mushroom Agaricus bisporus: biochemical and molecular characterization (1999)

Kersten, M. A. S. H. ; Müller, Y. ; Baars, J. J. P. ; [et al.]

Springer

Molecular genetics and genomics 261 (1999), S. 452-462

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ISSN: 1617-4623

Keywords: Key wordsAgarcius bisporus ; NAD+-specific glutamate dehydrogenase ; Molecular cloning ; Gene structure

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The NAD+-dependent glutamate dehydrogenase (NAD-GDH) of Agaricus bisporus, a key enzyme in nitrogen metabolism, was purified to homogeneity. The apparent molecular mass of the native enzyme is 474 kDa comprising four subunits of 116 kDa. The isoelectric point of the enzyme is about 7.0. K m values for ammonium, 2-oxoglutarate, NADH, glutamate and NAD+ were 6.5, 3.5, 0.06, 37.1 and 0.046 mM, respectively. The enzyme is specific for NAD(H). The gene encoding this enzyme (gdhB) was isolated from an A. bisporus H39 recombinant λ phage library. The deduced amino acid sequence specifies a 1029-amino acid protein with a deduced molecular mass of 115,463 Da, which displays a significant degree of similarity with NAD-GDH of Saccharomyces cerevisiae and Neurospora crassa. The ORF is interrupted by fifteen introns. Northern analysis combined with enzyme activity measurements suggest that NAD-GDH from A. bisporus is regulated by the nitrogen source. NAD-GDH levels in mycelium grown on glutamate were higher than NAD-GDH levels in mycelium grown on ammonium as a nitrogen source. Combined with the kinetic parameters, these results suggest a catabolic role for NAD-GDH. However, upon addition of ammonium to the culture transcription of the gene is not repressed as strongly as that of the gene encoding NADP-GDH (gdhA). To date, tetrameric NAD-GDHs with large subunits, and their corresponding genes, have only been isolated from a few species. This enzyme represents the first NAD-GDH of basidiomycete origin to be purified and is the first such enzyme from basidiomycetes whose sequence has been determined.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s004380050988

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Cloning, sequence and expression of the gene coding for rhamnogalacturonase ofAspergillus aculeatus; a novel pectinolytic enzyme (1995)

Suykerbuyk, M. E. G. ; Schaap, P. J. ; Stam, H. ; [et al.]

Springer

Applied microbiology and biotechnology 43 (1995), S. 861-870

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ISSN: 1432-0614

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Abstract Rhamnogalacturonase was purified from culture filtrate ofAspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The clonedrhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites forN-glycosylation. Limited homology withA. niger polygalacturonase amino acid sequences is found. A genomic clone ofrhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purifiedA. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence ofrhgA.A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either theA. niger pyrA gene or theA. aculeatus pyr A gene as selection marker. For expression of rhamnogalacturonase inA. awamori theA. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02431920

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Cloning, sequence and expression of the gene coding for rhamnogalacturonase of Aspergillus aculeatus; a novel pectinolytic enzyme (1995)

Suykerbuyk, M. E. G. ; Schaap, P. J. ; Stam, H. ; [et al.]

Springer

Applied microbiology and biotechnology 43 (1995), S. 861-870

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ISSN: 1432-0614

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Abstract Rhamnogalacturonase was purified from culture filtrate of Aspergillus aculeatus after growth in medium with sugar-beet pulp as carbon source. Purified protein was used to raise antibodies in mice and with the antiserum obtained a gene coding for rhamnogalacturonase (rhgA) was isolated from a λ cDNA expression library. The cloned rhgA gene has an open-reading frame of 1320 base pairs encoding a protein of 440 amino acids with a predicted molecular mass of 45 962 Da. The protein contains a potential signal peptidase cleavage site behind Gly-18 and three potential sites for N-glycosylation. Limited homology with A. niger polygalacturonase amino acid sequences is found. A genomic clone of rhgA was isolated from a recombinant phage λ genomic library. Comparison of the genomic and cDNA sequences revealed that the coding region of the gene is interrupted by three introns. Furthermore, amino acid sequences of four different peptides, derived from purified A. aculeatus rhamnogalacturonase, were also found in the deduced amino acid sequence of rhgA. A. aculeatus strains overexpressing rhamnogalacturonase were obtained by cotransformation using either the A. niger pyrA gene or the A. aculeatus pyrA gene as selection marker. For expression of rhamnogalacturonase in A. awamori the A. awamori pyrA gene was used as selection marker. Degradation patterns of modified hairy regions, determined by HPLC, show the recombinant rhamnogalacturonase to be active, and the enzyme was found to have a positive effect in the apple hot-mash liquefaction process.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s002530050497

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Nucleotide sequence and expression of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) fromAgaricus bisporus (1996)

Schaap, P. J. ; Müller, Y. ; Visser, J. ; [et al.]

Springer

Molecular genetics and genomics 250 (1996), S. 339-347

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ISSN: 1617-4623

Keywords: Agaricus bisporus ; NADP+-dependent glutamate dehydrogenase ; Molecular cloning ; Gene structure ; Mushroom

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) was isolated from anAgaricus bisporus recombinant phageλ library. The deduced amino acid sequence would specify a 457-amino acid protein that is highly homologous in sequence to those derived from previously isolated and characterized genes coding for microbial NADP+-GDH. The open reading frame is interrupted by six introns. None of the introns is located at either one of the positions of the two introns conserved in the corresponding open reading frames of the ascomycete fungiAspergillus nidulans andNeurospora crassa. Northern analysis suggests that theA. bisporus gdhA gene is transcriptionally regulated and that, unlike the case in ascomycetes, transcription of this gene is repressed upon the addition of ammonium to the culture.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02174392

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Nucleotide sequence and expression of the gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) from Agaricus bisporus (1996)

Schaap, P. J. ; Müller, Y. ; Baars, J. J. P. ; [et al.]

Springer

Molecular genetics and genomics 250 (1996), S. 339-347

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ISSN: 1617-4623

Keywords: Key words Agaricus bisporus ; NADP+-dependent glutamate dehydrogenase ; Molecular cloning ; Gene structure ; Mushroom

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The gene encoding NADP+-dependent glutamate dehydrogenase (gdhA) was isolated from an Agaricus bisporus recombinant phage λ library. The deduced amino acid sequence would specify a 457-amino acid protein that is highly homologous in sequence to those derived from previously isolated and characterized genes coding for microbial NADP+-GDH. The open reading frame is interrupted by six introns. None of the introns is located at either one of the positions of the two introns conserved in the corresponding open reading frames of the ascomycete fungi Aspergillus nidulans and Neurospora crassa. Northern analysis suggests that the A. bisporus gdhA gene is transcriptionally regulated and that, unlike the case in ascomycetes, transcription of this gene is repressed upon the addition of ammonium to the culture.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02174392

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